Year-end Sale % OFF 
Abstract
The Fab fragment of a rat monoclonal antibody (no. 192) with very high affinity for the main immunogenic region of the human muscle nicotinic acetylcholine receptor (AChR) has been purified, characterised and crystallised using vapour diffusion techniques. Its Kd for human AChR was determined to be 5×10 −11 M. Its cross-reactivity pattern suggests that residue α23 of the AChR strongly affects its epitope. Crystals suitable for X-ray analysis, obtained by micro- and macroseeding techniques, belong to the orthorhombic space group C222 1 and they diffract to 2.8 A resolution using synchrotron radiation. The unit cell dimensions are α = 83.4 Å, b =110.0 A ̊ and c = 212.2 A ̊ and there are two Fab molecules per asymmetric unit.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
